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Entry: Q9D9M9_MOUSE
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ID   Q9D9M9_MOUSE            Unreviewed;       248 AA.
AC   Q9D9M9;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF138 {ECO:0000256|ARBA:ARBA00039332};
DE   AltName: Full=RING finger protein 138 {ECO:0000256|ARBA:ARBA00041652};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF138 {ECO:0000256|ARBA:ARBA00041476};
GN   Name=Rnf138rt1 {ECO:0000313|Ensembl:ENSMUSP00000139291.2,
GN   ECO:0000313|MGI:MGI:1921514};
GN   Synonyms=1700045I19Rik {ECO:0000313|MGI:MGI:1921514};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAB24708.1};
RN   [1] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T.,
RA   Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T.,
RA   Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y.,
RA   Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C.,
RA   Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K.,
RA   Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M.,
RA   Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T.,
RA   Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAB24708.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB24708.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:BAB24708.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [9] {ECO:0000313|Ensembl:ENSMUSP00000139291.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139291.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [10] {ECO:0000313|Ensembl:ENSMUSP00000139291.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139291.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; AK006700; BAB24708.1; -; mRNA.
DR   RefSeq; NP_083118.1; NM_028842.3.
DR   STRING; 10090.ENSMUSP00000139291; -.
DR   PaxDb; 10090-ENSMUSP00000139291; -.
DR   DNASU; 74264; -.
DR   Ensembl; ENSMUST00000059320.4; ENSMUSP00000139291.2; ENSMUSG00000083695.7.
DR   GeneID; 74264; -.
DR   KEGG; mmu:74264; -.
DR   UCSC; uc009uuv.2; mouse.
DR   AGR; MGI:1921514; -.
DR   CTD; 74264; -.
DR   MGI; MGI:1921514; Rnf138rt1.
DR   VEuPathDB; HostDB:ENSMUSG00000083695; -.
DR   eggNOG; ENOG502RP2G; Eukaryota.
DR   GeneTree; ENSGT00950000182909; -.
DR   HOGENOM; CLU_092448_0_0_1; -.
DR   OMA; DCPLCEE; -.
DR   OrthoDB; 26661at2759; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 74264; 4 hits in 73 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000083695; Expressed in spermatid and 34 other cell types or tissues.
DR   GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; ISO:MGI.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR   CDD; cd16544; RING-HC_RNF138; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR034734; ZF_C2HC_RNF.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46968; E3 UBIQUITIN-PROTEIN LIGASE RNF138; 1.
DR   PANTHER; PTHR46968:SF1; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   Pfam; PF05605; zf-Di19; 1.
DR   Pfam; PF18574; zf_C2HC_14; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          19..59
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          87..106
FT                   /note="C2HC RNF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51803"
FT   REGION          124..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   248 AA;  28389 MW;  9C8207AF84C6C466 CRC64;
     MAEEESASTT SYTEDDFYCP ICQEVFKTPV RVAACKHVFC RKCFLSAMKE SRLHCPLCRG
     NVTRRERACP VRAVDLETIM RHFPGNCRCC SQRVELYRMR QHYKTCEKYQ DEFGVSTSVS
     SFQQSPNSVG NSNNEAPASA NAEVLQEEEE NASPPDEPTF DCPLCEEVTM SRQRLLDHCN
     SSHRGRVVSV TCPICLSLPW GDPPQLTRNF VSHLNQRHQF DYGDFVNLQL DEETQFQIAI
     EESFHVNI
//
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